ID A0A162C9P1_9CRUS Unreviewed; 457 AA.
AC A0A162C9P1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Anoctamin {ECO:0000256|RuleBase:RU280814};
GN ORFNames=APZ42_021767 {ECO:0000313|EMBL:KZS13162.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS13162.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS13162.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS13162.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS13162.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU280814}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU280814}.
CC -!- SIMILARITY: Belongs to the anoctamin family.
CC {ECO:0000256|ARBA:ARBA00009671, ECO:0000256|RuleBase:RU280814}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU280814}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZS13162.1}.
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DR EMBL; LRGB01001258; KZS13162.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162C9P1; -.
DR STRING; 35525.A0A162C9P1; -.
DR EnsemblMetazoa; XM_032925004.2; XP_032780895.1; LOC116919124.
DR Proteomes; UP000076858; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR InterPro; IPR032394; Anoct_dimer.
DR InterPro; IPR007632; Anoctamin.
DR InterPro; IPR049452; Anoctamin_TM.
DR PANTHER; PTHR12308; ANOCTAMIN; 1.
DR PANTHER; PTHR12308:SF84; ANOCTAMIN; 1.
DR Pfam; PF16178; Anoct_dimer; 1.
DR Pfam; PF04547; Anoctamin; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU280814};
KW Reference proteome {ECO:0000313|Proteomes:UP000076858};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU280814};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU280814}.
FT TRANSMEM 317..344
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 396..415
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT DOMAIN 36..303
FT /note="Anoctamin dimerisation"
FT /evidence="ECO:0000259|Pfam:PF16178"
FT DOMAIN 306..445
FT /note="Anoctamin transmembrane"
FT /evidence="ECO:0000259|Pfam:PF04547"
FT REGION 59..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 53031 MW; F867876F647FB64E CRC64;
MVFALQHIVV EPLPEVQDEC SRNGKQVKHP KSIGTYFRDG RRKIDYVLVH EEVSLAPSRS
RNHNTTIQSS LPLPFRPEEK SLQGGMRPTP LTSTIHQNTP KQNRKIDTRK TFIDKLKSQG
IEIEEEFAEG KRTNVRFIKL HAPFPLLAHW AEELGFRARI LCQAKAEEDN WSARLFKSLR
LPNCFAQEIP GDPPKVCCTY PFRRSKIATL LGNLDSESYF TSTERSRIVN EILARTTYGD
RRKGEVGIER LLKEGVYTAS YPLHEGCFHR KVNGNEDQEK LNPRQILHGY WARWSKWSKY
QPLDNVREYF GEKIAFYFAW LGFYTGWLIP PSIVGVLIFV YGLLTVDEDP ASSQVCRSIG
QYPMCPLCEE SQGCHQWDLS DVCTYSKLSY LFDHPGTVAF AIFVSFWAVT FLEYWKRYSA
RLAHRWDVVD VEREEIRPRP EFALKVLLLQ KLCQLNE
//
